Cytochrome bc1 complex: Difference between revisions

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'''Cytochrome bc1''' (Cbc1) functions as the central pump which transfers protons across the cell membrane.  The protons are used to power the rotation of ATP synthase.  Cbc1 binds ubiquinol which carries hydrogen atoms.  Cbc1 separates the protons and the electrons.  The protons are released in the inner side of the membrane for use by ATP synthase and the electrons are transferred to cytochrome c or to the outer side of the membrane.  Cbc1 is a dimeric protein composed of 11 proteins and cofactors which include heme and iron-sulfur cluster.  Plants use cytochrome b6f in the same manner binding plastoquinol as a hydrogen carrier.  Stigmatellin is an inhibitor of the Cbc1 electron transfer by binding to its quinone oxidation site.  Antimycin inhibits Cbc1 by binding to its quinone reduction site.
'''Cytochrome bc1''' (Cbc1) functions as the central pump which transfers protons across the cell membrane.  The protons are used to power the rotation of ATP synthase.  Cbc1 binds ubiquinol which carries hydrogen atoms.  Cbc1 separates the protons and the electrons.  The protons are released in the inner side of the membrane for use by ATP synthase and the electrons are transferred to cytochrome c or to the outer side of the membrane.  Cbc1 is a dimeric protein composed of 11 proteins and cofactors which include heme-carrying proteins like cytochrome b (Cb) and cytochrome c1 (Cc1) and iron-sulfur cluster proteins like Rieske Fe-S protein (RISP).  Plants use cytochrome b6f in the same manner binding plastoquinol as a hydrogen carrier.  Stigmatellin is an inhibitor of the Cbc1 electron transfer by binding to its quinone oxidation site.  Antimycin inhibits Cbc1 by binding to its quinone reduction site.


Cytochrome bc1 in [[Complex_III_of_Electron_Transport_Chain|complex III]] of the mitochondrial electron transport chain.   
Cytochrome bc1 in [[Complex_III_of_Electron_Transport_Chain|complex III]] of the mitochondrial electron transport chain.   
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


[[1bcc]] – cCbc1 + ubiquinone-10 + heme + Fe2S2 chicken<br />
[[2fyn]] - RsCb (mutant) + Cc1 + RISP Rhodobacter sphaeroides<BR />
[[3bcc]], [[3h1i]] – cCbc1 + stigmatellin + antimycin + heme + Fe2S2<BR />
[[1zrt]] - Cb + Cc1 + RISP Rhodobacter capsulatus<BR />
[[2bcc]] - cCbc1 + ubiquinone-10 + stigmatellin + heme + Fe2S2<BR />
[[1bgy]], [[1be3]], [[1l0n]], [[1ntm]] - bCb + bCc1 + RISP bovine <BR />
[[3h1h]] - cCbc1 + ubiquinone-10 + heme + Fe2S2<BR />
[[1qcr]] - bCb + bCc1 + RISP – Cα model<BR />
[[1qcr]] – bCbc1 (Cα atoms) + heme - bovine<br />
[[1sqp]], [[2fyu]], [[1l0l]], [[1ntk]], [[1pp9]], [[1ppj]], [[1sqb]], [[2a06]], [[1sqv]], [[1sqx]], [[1sqq]] - bCb + bCc1 + RISP + inhibitor<BR />
[[1bgy]], [[1be3]] - bCbc1 + heme + Fe2S2<BR />
[[1ntz]] - bCb + bCc1 + RISP + ubiquinone<BR />
[[1pp9]], [[2a06]] - bCbc1 + ubiquinone-10 + stigmatellin + heme + Fe2S2<BR />
[[1nu1]] - bCb + bCc1 + RISP + quinolone derivative<BR />
[[1ppj]] - bCbc1 + stigmatellin + antimycin + heme + Fe2S2<BR />
[[2qjk]] - RsCb (mutant) + RsCc1 + RISP + inhibitor<BR />
[[2qjp]] - RsCb + RsCc1 + RISP + inhibitor<BR />
[[2qjy]] - RsCb (mutant) + RsCc1 + RISP (mutant) + inhibitor<BR />
[[2ibz]], [[1kyo]], [[1kb9]], [[1p84]] - yCb + yCc1 + RISP + inhibitor - yeast<BR />
[[3cx5]] - yCb + yCc1 + RISP <BR />
[[1ezv]] - yCb + yCc1 + RISP + antibody<BR />
[[2yiu]] - Cb + Cc1 + RISP – Paracoccus denitrificans<BR />
[[1qcr]] - bCb + bCc1 + RISP – bovine – Cα model<BR />
[[3cxh]], [[3h1h]], [[1bcc]], [[3h1h]] - cCb + cCc1 + RISP - chicken<BR />
[[3cwb]], [[3h1i]], [[3h1j]], [[3h1k]], [[3h1l]], [[3l70]], [[3l71]], [[3l72]], [[3l73]], [[3l74]], [[3l75]], [[3tgu]], [[3bcc]], [[2bcc]], [[3h1i]] - cCb + cCc1 + RISP + inhibitor<BR />
 
 
 
 
 


[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Karl Oberholser, Jaime Prilusky, Joel L. Sussman